4o1f: Difference between revisions
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==Structure of a methyltransferase component in complex with THF involved in O-demethylation== | ==Structure of a methyltransferase component in complex with THF involved in O-demethylation== | ||
<StructureSection load='4o1f' size='340' side='right' caption='[[4o1f]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4o1f' size='340' side='right' caption='[[4o1f]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4o1f]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O1F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O1F FirstGlance]. <br> | <table><tr><td colspan='2'>[[4o1f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Deshd Deshd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O1F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O1F FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o0q|4o0q]], [[4o1e|4o1e]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o0q|4o0q]], [[4o1e|4o1e]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1f OCA], [http://pdbe.org/4o1f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o1f RCSB], [http://www.ebi.ac.uk/pdbsum/4o1f PDBsum]</span></td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dhaf_0722 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272564 DESHD])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1f OCA], [http://pdbe.org/4o1f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o1f RCSB], [http://www.ebi.ac.uk/pdbsum/4o1f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1f ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4o1f" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4o1f" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Deshd]] | |||
[[Category: Dunstan, M S]] | [[Category: Dunstan, M S]] | ||
[[Category: Fisher, K]] | [[Category: Fisher, K]] | ||
Revision as of 20:37, 16 November 2017
Structure of a methyltransferase component in complex with THF involved in O-demethylationStructure of a methyltransferase component in complex with THF involved in O-demethylation
Structural highlights
Publication Abstract from PubMedO-Demethylation by acetogenic or organohalide-respiring bacteria leads to the formation of methyltetrahydrofolate from aromatic methyl ethers. O-Demethylases, which are cobalamin-dependent, three-component enzyme systems, catalyse methyl-group transfers from aromatic methyl ethers to tetrahydrofolate via methylcobalamin intermediates. In this study, crystal structures of the tetrahydrofolate-binding methyltransferase module from a Desulfitobacterium hafniense DCB-2 O-demethylase were determined both in complex with tetrahydrofolate and the product methyltetrahydrofolate. While these structures are similar to previously determined methyltransferase structures, the position of key active-site residues is subtly altered. A strictly conserved Asn is displaced to establish a putative proton-transfer network between the substrate N5 and solvent. It is proposed that this supports the efficient catalysis of methyltetrahydrofolate formation, which is necessary for efficient O-demethylation. Structures of the methyltransferase component of Desulfitobacterium hafniense DCB-2 O-demethylase shed light on methyltetrahydrofolate formation.,Sjuts H, Dunstan MS, Fisher K, Leys D Acta Crystallogr D Biol Crystallogr. 2015 Sep 1;71(Pt 9):1900-8. doi:, 10.1107/S1399004715013061. Epub 2015 Aug 25. PMID:26327380[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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